InterPro domain: IPR016657

This group represents a phosphoacetylglucosamine mutase (PAGM; also known as phosphoglucomutase 3 or N-acetylglucosamine-phosphate mutase [ 1 ]). It is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. PAGM is a member of the alpha-D-phosphohexomutase superfamily [ 2 ], which catalyzes the intramolecular phosphoryl transfer of sugar substrates [ 3 ]. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain [ 4 ]. All four domains are included in this alignment model.

1. Identification of human phosphoglucomutase 3 (PGM3) as N-acetylglucosamine-phosphate mutase (AGM1). Ann. Hum. Genet. 66, 139-44
2. Crystal structures of N-acetylglucosamine-phosphate mutase, a member of the alpha-D-phosphohexomutase superfamily, and its substrate and product complexes. J. Biol. Chem. 281, 19740-7
3. Agm1/Pgm3-mediated sugar nucleotide synthesis is essential for hematopoiesis and development. Mol. Cell. Biol. 27, 5849-59
4. Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis. Biochim. Biophys. Acta 1492, 369-76